| Description | The biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. The 80 residues surrounding the biotinyl-binding lysine residue display some sequence similarity to that around the lipoyl-binding lysine residue. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [ ]. E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group []. The lipoic acid cofactor is found in a variety of proteins that include, H-protein of the glycine cleavage system (GCS), mammalian and yeast pyruvate dehydrogenases and branched-chain 2-oxo acid dehydrogenase complex (BCOADC).The lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes and the biotinyl domains of biotin-dependent enzymes have been solved, which revealed that they have homologous structures consisting of a flattened 8-stranded -barrel with the target lysine positioned in comparable β-turns. Additional important residues for specificity have been identified, such as the conserved methionine flanking the target lysine that is essential for the recognition of the biotinyl domain by the biotinyl protein ligase [ , ]. | Name | Biotin/lipoyl attachment |
| Short Name | Biotin_lipoyl | Type | Domain |
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